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Fractionation of whole casein on hydroxyapatite. Application to a study of buffalo κ-casein

Published online by Cambridge University Press:  01 June 2009

F. Addeo ,
J.-M. Chobert  and
B. Ribadeau-Dumas
F. Addeo
Affiliation:
Laboratoire de Recherches sur les Protéines, Institut National de la Recherche Agronomique, CRNZ, 78350-Jouy-en-Josas, France
J.-M. Chobert
Affiliation:
Laboratoire de Recherches sur les Protéines, Institut National de la Recherche Agronomique, CRNZ, 78350-Jouy-en-Josas, France
B. Ribadeau-Dumas
Affiliation:
Laboratoire de Recherches sur les Protéines, Institut National de la Recherche Agronomique, CRNZ, 78350-Jouy-en-Josas, France
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Summary

When whole caseins from cow and Italian buffalo (Bubalus arnee) were fractionated by chromatography on a column of hydroxyapatite they behaved in a similar manner. κ-Casein was eluted with 5 mM phosphate buffer, pH 6·8, containing 0·2 M-KCI, 4·5 M-urea and 2 mM-2-mercaptoethanol, but β- and αs-caseins were retained and could be eluted successively by a linear gradient from 5 mM to 250 mMphosphate buffer. Buffalo κ-casein preparations, obtained from bulk milk or from milks of individual animals by chromatography on hydroxyapatite, produced identical electrophoretic patterns at pH 8·6. By further fractionation of these κ-caseins on DEAE-cellulose, in each case, at least 7 components were purified; they had different electrophoretic mobilities but were all sensitive towards chymosin. The major fraction migrated like component 1 of bovine κ-casein B.

Type
Original Articles
Information
Journal of Dairy Research , Volume 44 , Issue 1 , February 1977 , pp. 63 - 68
Copyright
Copyright © Proprietors of Journal of Dairy Research 1977

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References

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